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Gene Review

SERINC5  -  serine incorporator 5

Homo sapiens

Synonyms: C5orf12, Serine incorporator 5, TPO1
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Disease relevance of SERINC5

  • This suggests that TPO1 catalyzes polyamine excretion at acidic pH, similar to the PotE transporter in Escherichia coli [1].

High impact information on SERINC5

  • Using specific oligonucleotide probes for the mRNAs derived from the cDNA sequences hTPO-1 and hTPO-2, we show that both are expressed in all thyroid tissues examined and the relative level of two mRNAs is different in each sample [2].
  • The transport activity of TPO1 was enhanced through phosphorylation at Ser19 by protein kinase C and at Thr52 by casein kinase 1 [1].
  • When expressed from a multi-copy vector, TPO1 was located mainly on the plasma membrane, but with some localization on the vacuolar membrane [1].
  • Paraquat, a polyamine analogue, was excreted by TPO1 at a rate comparable with the excretion of spermidine (deduced from the inhibition of spermidine uptake) at pH 5 [1].
  • This shows that both forms of TPO contain exon 10-encoded polypeptide of TPO-1 [3].

Biological context of SERINC5

  • Furthermore, we confirm that both the larger and smaller forms of TPO observed on gel electrophoresis contain TPO-1, suggesting that the difference is caused by posttranslational modifications [3].
  • The results of pulse chase and cell surface biotinylation experiments showed that the TPOzanelli has a shorter half-life (7 versus 11 h) and is expressed at the cell surface in lesser amounts than TPO1 (7 versus 15%) [4].

Anatomical context of SERINC5

  • The result showed that C5orf12 was highly expressed in placenta, skeletal muscle, spleen, thymus, testis and peripheral leukocyte while expressed weakly in heart and liver [5].
  • The total enzymatic activity and cell surface activity were determined in CHO cells expressing TPO1 and TPOzanelli, and TPO1 and TPOzanelli were found to have similar levels of activity [4].

Physical interactions of SERINC5

  • The binding of anti-exon 10 peptide antibodies to the immunodepleted TPO-1 fraction was considerably diminished in comparison to binding of polyclonal anti-TPO, suggesting the presence of small amounts (< 10%) of TPO-2 expressed as a protein in thyroid cells [3].

Analytical, diagnostic and therapeutic context of SERINC5

  • There were 6 PCR products differing in size; sequence analysis showed the full-length TPO mRNA (TPO-1), 12- and 116-bp deleted variants (TPO-2 and TPO-3, respectively), and 3 novel isoforms (197- and 128-bp deleted forms and a 60-bp insert form of TPO-3; named TPO-4, TPO-5, and TPO-6, respectively) [6].
  • No TPO-1 (wild-type) protein was detected by Western blotting [7].
  • In addition to the full length molecule of 933 amino acids (TPO1), Northern blotting and sequencing have revealed several shorter transcripts [8].


  1. Characteristics of the polyamine transporter TPO1 and regulation of its activity and cellular localization by phosphorylation. Uemura, T., Tachihara, K., Tomitori, H., Kashiwagi, K., Igarashi, K. J. Biol. Chem. (2005) [Pubmed]
  2. Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. Kimura, S., Kotani, T., McBride, O.W., Umeki, K., Hirai, K., Nakayama, T., Ohtaki, S. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  3. Human thyroid peroxidase (TPO) isoforms, TPO-1 and TPO-2: analysis of protein expression in Graves' thyroid tissue. Gardas, A., Lewartowska, A., Sutton, B.J., Pasieka, Z., McGregor, A.M., Banga, J.P. J. Clin. Endocrinol. Metab. (1997) [Pubmed]
  4. Alternatively spliced form of human thyroperoxidase, TPOzanelli: activity, intracellular trafficking, and role in hormonogenesis. Niccoli-Sire, P., Fayadat, L., Siffroi-Fernandez, S., Malthierry, Y., Franc, J.L. Biochemistry (2001) [Pubmed]
  5. Cloning and expression of a novel human C5orf12 gene*, a member of the TMS_TDE family. Xu, J., Ji, C., Wang, L., Cao, Y., Dai, J., Ye, X., Zeng, L., Dai, J., Wu, Q., Xie, Y., Mao, Y. Mol. Biol. Rep. (2003) [Pubmed]
  6. Production of thrombopoietin by human carcinomas and its novel isoforms. Sasaki, Y., Takahashi, T., Miyazaki, H., Matsumoto, A., Kato, T., Nakamura, K., Iho, S., Okuno, Y., Nakao, K. Blood (1999) [Pubmed]
  7. Congenital hypothyroidism caused by a premature termination signal in exon 10 of the human thyroid peroxidase gene. Bikker, H., Waelkens, J.J., Bravenboer, B., de Vijlder, J.J. J. Clin. Endocrinol. Metab. (1996) [Pubmed]
  8. The thyroperoxidase doublet is not produced by alternative splicing. Cetani, F., Costagliola, S., Tonacchera, M., Panneels, V., Vassart, G., Ludgate, M. Mol. Cell. Endocrinol. (1995) [Pubmed]
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